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| pubmed-article:8132516 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:8132516 | lifeskim:mentions | umls-concept:C0034826 | lld:lifeskim |
| pubmed-article:8132516 | lifeskim:mentions | umls-concept:C0063592 | lld:lifeskim |
| pubmed-article:8132516 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
| pubmed-article:8132516 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
| pubmed-article:8132516 | lifeskim:mentions | umls-concept:C1514758 | lld:lifeskim |
| pubmed-article:8132516 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:8132516 | pubmed:dateCreated | 1994-4-18 | lld:pubmed |
| pubmed-article:8132516 | pubmed:abstractText | Stimulation of SH-SY5Y human neuroblastoma cells with carbachol, a muscarinic agonist, down-regulates the type I inositol 1,4,5-trisphosphate (InsP3) receptor by > 90% with maximal and half-maximal effects after approximately 6 h and approximately 1 h, respectively. Examination of the mechanistic basis of this down-regulation revealed that carbachol increased the rate of type I InsP3 receptor degradation (radiolabeled immunoprecipitable receptor was lost from cells with half-times of > 8 h and approximately 1 h in the absence and presence of carbachol, respectively) and that the concentration of type I InsP3 receptor mRNA, despite a transient decrease after 3 h, did not correlate with levels of the receptor. Only those muscarinic receptor subtypes coupled to stimulation of phosphoinositide hydrolysis were capable of causing type I InsP3 receptor down-regulation. Ca2+ mobilization was pivotal to the mechanisms of receptor down-regulation, since perturbation of Ca2+ homeostasis with either EGTA or thapsigargin blocked the ability of carbachol to accelerate receptor degradation. Studies with thapsigargin also revealed that both functional InsP3-sensitive Ca2+ stores and persistent elevation of InsP3 concentration were required for down-regulation to occur. In conclusion, phosphoinositidase C-linked muscarinic receptors down-regulate the type I InsP3 receptor by accelerating its degradation. It appears that this process is initiated by persistent discharge of intracellular Ca2+ stores via the channels formed by tetramerically complexed type I InsP3 receptors. | lld:pubmed |
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| pubmed-article:8132516 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8132516 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8132516 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8132516 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:8132516 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8132516 | pubmed:author | pubmed-author:NahorskiS RSR | lld:pubmed |
| pubmed-article:8132516 | pubmed:author | pubmed-author:MikoshibaKK | lld:pubmed |
| pubmed-article:8132516 | pubmed:author | pubmed-author:WojcikiewiczR... | lld:pubmed |
| pubmed-article:8132516 | pubmed:author | pubmed-author:NakadeSS | lld:pubmed |
| pubmed-article:8132516 | pubmed:author | pubmed-author:FuruichiTT | lld:pubmed |
| pubmed-article:8132516 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8132516 | pubmed:day | 18 | lld:pubmed |
| pubmed-article:8132516 | pubmed:volume | 269 | lld:pubmed |
| pubmed-article:8132516 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8132516 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8132516 | pubmed:pagination | 7963-9 | lld:pubmed |
| pubmed-article:8132516 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:8132516 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8132516 | pubmed:articleTitle | Muscarinic receptor activation down-regulates the type I inositol 1,4,5-trisphosphate receptor by accelerating its degradation. | lld:pubmed |
| pubmed-article:8132516 | pubmed:affiliation | Department of Cell Physiology and Pharmacology, University of Leicester. | lld:pubmed |
| pubmed-article:8132516 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8132516 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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